Literature DB >> 24510918

Slippery substrates impair ATP-dependent protease function by slowing unfolding.

Philip Coffino1, Priscilla Hiu-Mei Too, Jenny Erales.   

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Year:  2014        PMID: 24510918      PMCID: PMC3916579          DOI: 10.1074/jbc.L113.532622

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


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  5 in total

1.  Repeat sequence of Epstein-Barr virus-encoded nuclear antigen 1 protein interrupts proteasome substrate processing.

Authors:  Mingsheng Zhang; Philip Coffino
Journal:  J Biol Chem       Date:  2003-12-19       Impact factor: 5.157

2.  Slippery substrates impair ATP-dependent protease function by slowing unfolding.

Authors:  Daniel A Kraut
Journal:  J Biol Chem       Date:  2013-10-22       Impact factor: 5.157

3.  Sequence- and species-dependence of proteasomal processivity.

Authors:  Daniel A Kraut; Eitan Israeli; Erin K Schrader; Ashwini Patil; Kenta Nakai; Dhaval Nanavati; Tomonao Inobe; Andreas Matouschek
Journal:  ACS Chem Biol       Date:  2012-06-28       Impact factor: 5.100

4.  Glycine-alanine repeats impair proper substrate unfolding by the proteasome.

Authors:  Martin A Hoyt; Judith Zich; Junko Takeuchi; Mingsheng Zhang; Cedric Govaerts; Philip Coffino
Journal:  EMBO J       Date:  2006-04-06       Impact factor: 11.598

5.  Slippery substrates impair function of a bacterial protease ATPase by unbalancing translocation versus exit.

Authors:  Priscilla Hiu-Mei Too; Jenny Erales; Joana Danica Simen; Antonija Marjanovic; Philip Coffino
Journal:  J Biol Chem       Date:  2013-03-25       Impact factor: 5.157

  5 in total
  2 in total

1.  Reply to Coffino et al.: slippery substrates impair ATP-dependent protease function by slowing unfolding.

Authors:  Daniel A Kraut
Journal:  J Biol Chem       Date:  2014-02-07       Impact factor: 5.157

Review 2.  The Logic of the 26S Proteasome.

Authors:  Galen Andrew Collins; Alfred L Goldberg
Journal:  Cell       Date:  2017-05-18       Impact factor: 41.582

  2 in total

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